Purification, characterization, and crystallization of an N-hydroxyarylamine O-acetyltransferase from Salmonella typhimurium.

@article{Sinclair1998PurificationCA,
  title={Purification, characterization, and crystallization of an N-hydroxyarylamine O-acetyltransferase from Salmonella typhimurium.},
  author={John C. Sinclair and Rupika Delgoda and Martin E.M Noble and Sarah J Jarmin and Ngoh Khang Goh and E Sim},
  journal={Protein expression and purification},
  year={1998},
  volume={12 3},
  pages={371-80}
}
The N-hydroxyarylamine O-acetyltransferase from Salmonella typhimurium has been expressed as a histidine-tagged fusion protein in Escherichia coli and purified to apparent homogeneity using single-step immobilized metal ion chromatography. Sufficient quantities of the purified protein have been obtained to allow its characterization by physical methods including dynamic light scattering and electrospray mass spectrometry. The substrate specificity and temperature sensitivity of the enzymatic… CONTINUE READING

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